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Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure.
[epidermolysis bullosa simplex]
Plectin
,
a
cytolinker
of
the
plakin
family
,
anchors
the
intermediate
filament
(
IF
)
network
formed
by
keratins
5
and
14
(
K
5
/
K
14
)
to
hemidesmosomes
,
junctional
adhesion
complexes
in
basal
keratinocytes
.
Genetic
alterations
of
these
proteins
cause
epidermolysis
bullosa
simplex
(
EBS
)
characterized
by
disturbed
cytoarchitecture
and
cell
fragility
.
The
mechanisms
through
which
mutations
located
after
the
documented
plectin
IF-binding
site
,
composed
of
the
plakin-repeat
domain
(
PRD
)
B
5
and
the
linker
,
as
well
as
mutations
in
K
5
or
K
14
,
lead
to
EBS
remain
unclear
.
We
investigated
the
interaction
of
plectin
C
terminus
,
encompassing
four
domains
,
the
PRD
B
5
,
the
linker
,
the
PRD
C
,
and
the
C
extremity
,
with
K
5
/
K
14
using
different
approaches
,
including
a
rapid
and
sensitive
fluorescent
protein-binding
assay
,
based
on
enhanced
green
fluorescent
protein-tagged
proteins
(
FluoBACE
)
.
Our
results
demonstrate
that
all
four
plectin
C-
terminal
domains
contribute
to
its
association
with
K
5
/
K
14
and
act
synergistically
to
ensure
efficient
IF
binding
.
The
plectin
C
terminus
predominantly
interacted
with
the
K
5
/
K
14
coil
1
domain
and
bound
more
extensively
to
K
5
/
K
14
filaments
compared
with
monomeric
keratins
or
IF
assembly
intermediates
.
These
findings
indicate
a
multimodular
association
of
plectin
with
K
5
/
K
14
filaments
and
give
insights
into
the
molecular
basis
of
EBS
associated
with
pathogenic
mutations
in
plectin
,
K
5
,
or
K
14
genes
.
Diseases
Validation
Diseases presenting
"enhanced green fluorescent protein-tagged proteins"
symptom
epidermolysis bullosa simplex
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